The baculovirus-insect cell system is widely used to produce recombinant glycoproteins for diverse biomedical research projects and direct clinical applications. However, there are some key differences between insect and higher eukaryotic cellular protein glycosylation pathways, which can effectively preclude the use of recombinant glycoproteins produced in the baculovirus-insect cell system for some applications. One difference is that insect cell lines are generally unable to elongate trimmed N- and O-glycans to produce complex, terminally sialylated structures. Another is that some insect cell lines can produce highly immunogenic, core alpha-fucosylated N-glycans. cannot synthesize products with structurally authentic carbohydrate side chains. Our research focuses on efforts to elucidate and engineer protein glycosylation pathways in the baculovirus-insect cell system. This presentation will provide an overview of our recent glycoengineering efforts, which have yielded new baculovirus-insect cell systems with the ability to produce humanized, non-immunogenic recombinant glycoproteins.

Protein glycosylation in the baculovirus-insect cell system

249th National Meeting (2015)

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